The new coronavirus peplomer, which allows it to infect human cells, is a faster-spreading version of the virus, such as the one first reported in the United Kingdom and South Africa, compared to the original form of the pathogen from Wuhan. More stable in, China says new research.
Researchers, including researchers at Boston Children’s Hospital in the United States, have evaluated the structure of coronavirus peplomers to the atomic level and how they are altered by the D614G mutation carried by the Brazilian, South African, and British variants of SARS. discovered. -CoV-2 virus.
Results published in the journal Science showed that mutations stabilize spikes more than the original SARS-CoV-2 virus from Wuhan, allowing mutants to spread more quickly. .. According to scientists, the original viral spike protein binds to the ACE2 receptor in human cells and then dramatically transforms and folds, allowing the virus to fuse its membrane with the host cell.
However, they said the spikes could prematurely reshape and fall apart before the virus binds to the cells.
This slowed down the virus, but researchers say the change in shape also made it difficult for the human immune system to contain the virus.
“The original peplomer dissociated and was not sufficient to elicit a strong neutralizing antibody response,” said study co-author Bing Chen of Boston Children’s Hospital. In variants, scientists said that mutations block premature shape changes and stabilize spikes by binding them weaker to the ACE2 receptor.
Researchers say that these spikes are less likely to collapse prematurely, making the entire virus more infectious. “Suppose the original virus has 100 spikes. Due to its unstable shape, it may only work 50%. In the G614 variant, 90% may work, so Even if they don’t bind, they’re more likely to get infected, “Chen explains.
Based on the findings, scientists suggested that the redesigned vaccine incorporates the code for this mutant peplomer.
They believe that the more stable spike shape makes vaccines based on these viral proteins more likely to induce defense-neutralizing antibodies.
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